4p9t: Difference between revisions
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/CTNA2_MOUSE CTNA2_MOUSE]] May function as a linker between cadherin adhesion receptors and the cytoskeleton to regulate cell-cell adhesion and differentiation in the nervous system. Regulates morphological plasticity of synapses and cerebellar and hippocampal lamination during development. Functions in the control of startle modulation.<ref>PMID:12089526</ref> <ref>PMID:12123610</ref> <ref>PMID:15034585</ref> | [[http://www.uniprot.org/uniprot/CTNA2_MOUSE CTNA2_MOUSE]] May function as a linker between cadherin adhesion receptors and the cytoskeleton to regulate cell-cell adhesion and differentiation in the nervous system. Regulates morphological plasticity of synapses and cerebellar and hippocampal lamination during development. Functions in the control of startle modulation.<ref>PMID:12089526</ref> <ref>PMID:12123610</ref> <ref>PMID:15034585</ref> | ||
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== Publication Abstract from PubMed == | |||
The N-terminal vinculin-homology 1 (VH1) domain of alpha-catenin facilitates two exclusive forms, a monomeric form directly bound to beta-catenin for linking E-cadherin to F-actin or a homodimer for the inhibition of beta-catenin binding. Competition of these two forms is affected by approximately 80 N-terminal residues, whose structure is poorly understood. We have determined the structure of the monomeric free form of the alphaN-catenin VH1 domain and revealed that the N-terminal residues form alpha1 and alpha2 helices to complete formation of the N-terminal four-helix bundle. Dynamic conformational changes of these two helices control formation of the beta-catenin-bound monomer or unbound homodimer. | |||
Structure of the free form of the N-terminal VH1 domain of monomeric alpha-catenin.,Shibahara T, Hirano Y, Hakoshima T FEBS Lett. 2015 Jul 8;589(15):1754-60. doi: 10.1016/j.febslet.2015.05.053. Epub, 2015 Jun 9. PMID:26071377<ref>PMID:26071377</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 10:45, 15 July 2015
Structure of the free form of the N-terminal VH1 domain of monomeric alpha-cateninStructure of the free form of the N-terminal VH1 domain of monomeric alpha-catenin
Structural highlights
Function[CTNA2_MOUSE] May function as a linker between cadherin adhesion receptors and the cytoskeleton to regulate cell-cell adhesion and differentiation in the nervous system. Regulates morphological plasticity of synapses and cerebellar and hippocampal lamination during development. Functions in the control of startle modulation.[1] [2] [3] Publication Abstract from PubMedThe N-terminal vinculin-homology 1 (VH1) domain of alpha-catenin facilitates two exclusive forms, a monomeric form directly bound to beta-catenin for linking E-cadherin to F-actin or a homodimer for the inhibition of beta-catenin binding. Competition of these two forms is affected by approximately 80 N-terminal residues, whose structure is poorly understood. We have determined the structure of the monomeric free form of the alphaN-catenin VH1 domain and revealed that the N-terminal residues form alpha1 and alpha2 helices to complete formation of the N-terminal four-helix bundle. Dynamic conformational changes of these two helices control formation of the beta-catenin-bound monomer or unbound homodimer. Structure of the free form of the N-terminal VH1 domain of monomeric alpha-catenin.,Shibahara T, Hirano Y, Hakoshima T FEBS Lett. 2015 Jul 8;589(15):1754-60. doi: 10.1016/j.febslet.2015.05.053. Epub, 2015 Jun 9. PMID:26071377[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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